3B9N

Crystal structure of long-chain alkane monooxygenase (LadA)

Summary for 3B9N

• Entry DOI: 10.2210/pdb3b9n/pdb
• Related: 3B9O
• Descriptor: Alkane monooxygenase (2 entities in total)
• Functional Keywords: geobacillus thermodenitrificans, lada, alkane hydroxylase, monooxygenase, plasmid, oxidoreductase
• Biological source: Geobacillus thermodenitrificans
• Total number of polymer chains: 2
• Total formula weight: 101080.24

Authors

Li, L.,Yang, W.,Xu, F.,Bartlam, M.,Rao, Z. (deposition date: 2007-11-06, release date: 2008-01-15, Last modification date: 2023-11-01)

Primary citation

Li, L.,Liu, X.,Yang, W.,Xu, F.,Wang, W.,Feng, L.,Bartlam, M.,Wang, L.,Rao, Z.
Crystal structure of long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alkane hydroxylase
J.Mol.Biol., 376:453-465, 2008

PubMed Abstract: LadA, a long-chain alkane monooxygenase, utilizes a terminal oxidation pathway for the conversion of long-chain alkanes (up to at least C(36)) to corresponding primary alcohols in thermophilic bacillus Geobacillus thermodenitrificans NG80-2. Here, we report the first structure of the long-chain alkane hydroxylase, LadA, and its complex with the flavin mononucleotide (FMN) coenzyme. LadA is characterized as a new member of the SsuD subfamily of the bacterial luciferase family via a surprising structural relationship. The LadA:FMN binary complex structure and a LadA:FMN:alkane model reveal a hydrophobic cavity that has dual roles: to provide a hydrogen-bond donor (His138) for catalysis and to create a solvent-free environment in which to stabilize the C4a-hydroperoxyflavin intermediate. Consequently, LadA should catalyze the conversion of long-chain alkanes via the acknowledged flavoprotein monooxygenase mechanism. This finding suggests that the ability of LadA to catalyze the degradation of long-chain alkanes is determined by the binding mode of the long-chain alkane substrates. The LadA structure opens a rational perspective to explore and alter the substrate binding site of LadA, with potential biotechnological applications in areas such as petroleum exploration and treatment of environmental oil pollution.

PubMed: 18164311
DOI: 10.1016/j.jmb.2007.11.069

Experimental method

X-RAY DIFFRACTION (2.7 Å)